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O95147 (DUS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 14

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
MKP-1-like protein tyrosine phosphatase
Short name=MKP-L
Mitogen-activated protein kinase phosphatase 6
Short name=MAP kinase phosphatase 6
Short name=MKP-6
Gene names
Name:DUSP14
Synonyms:MKP6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with CD28.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Dual specificity protein phosphatase 14
PRO_0000094822

Regions

Domain91 – 15666Tyrosine-protein phosphatase

Sites

Active site1111Phosphocysteine intermediate Ref.5

Secondary structure

................................ 198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95147 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6AAFAE1B3A24F9AA

FASTA19822,255
        10         20         30         40         50         60 
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRGS VASNRHLLQA RGITCIVNAT 

        70         80         90        100        110        120 
IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV SRKHGATLVH CAAGVSRSAT 

       130        140        150        160        170        180 
LCIAYLMKFH NVCLLEAYNW VKARRPVIRP NVGFWRQLID YERQLFGKST VKMVQTPYGI 

       190 
VPDVYEKESR HLMPYWGI 

« Hide

References

« Hide 'large scale' references
[1]"MKP-L, a novel MKP-1 like protein tyrosine phosphatase."
Yuan Y., Suphapeetiporn K., Sun H.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6."
Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M., King P.D.
J. Immunol. 166:197-206(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Overproduction, purification and structure determination of human dual-specificity phosphatase 14."
Lountos G.T., Tropea J.E., Cherry S., Waugh D.S.
Acta Crystallogr. D 65:1013-1020(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-191 IN COMPLEX WITH PHOSPHATE, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038844 mRNA. Translation: AAD02105.1.
AF120032 mRNA. Translation: AAF28861.1.
BC000370 mRNA. Translation: AAH00370.1.
BC001894 mRNA. Translation: AAH01894.1.
BC004448 mRNA. Translation: AAH04448.1.
CCDSCCDS11320.1.
RefSeqNP_008957.1. NM_007026.3.
XP_005257034.1. XM_005256977.1.
XP_006725363.1. XM_006725300.1.
UniGeneHs.91448.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WGPX-ray1.88A/B2-191[»]
ProteinModelPortalO95147.
SMRO95147. Positions 24-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116255. 6 interactions.
IntActO95147. 1 interaction.
STRING9606.ENSP00000292964.

Chemistry

BindingDBO95147.
ChEMBLCHEMBL1764941.

PTM databases

PhosphoSiteO95147.

Proteomic databases

MaxQBO95147.
PaxDbO95147.
PeptideAtlasO95147.
PRIDEO95147.

Protocols and materials databases

DNASU11072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394386; ENSP00000377910; ENSG00000161326.
ENST00000394389; ENSP00000377912; ENSG00000161326.
ENST00000487847; ENSP00000466299; ENSG00000161326.
GeneID11072.
KEGGhsa:11072.
UCSCuc002hnx.2. human.

Organism-specific databases

CTD11072.
GeneCardsGC17P035850.
HGNCHGNC:17007. DUSP14.
HPAHPA019911.
MIM606618. gene.
neXtProtNX_O95147.
PharmGKBPA27523.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000233766.
HOVERGENHBG051422.
InParanoidO95147.
KOK14165.
OMAYLMKFHS.
OrthoDBEOG7PK90H.
PhylomeDBO95147.
TreeFamTF316009.

Gene expression databases

ArrayExpressO95147.
BgeeO95147.
CleanExHS_DUSP14.
GenevestigatorO95147.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95147.
GenomeRNAi11072.
NextBio42090.
PROO95147.
SOURCESearch...

Entry information

Entry nameDUS14_HUMAN
AccessionPrimary (citable) accession number: O95147
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM